Structure of PDB 3x1m Chain B

Receptor sequence
>3x1mB (length=158) Species: 350703 (Pseudomonas aeruginosa 2192) [Search protein sequence]
MNRVLYPGTFDPITKGHGDLIERASRLFDHVIIAVAASPKKNPLFSLEQR
VALAQEVTKHLPNVEVVGFSTLLAHFVKEQKANVFLRGLRAVSDFEYEFQ
LANMNRQLAPDVESMFLTPSEKYSFISSTLVREIAALGGDISKFVHPAVA
DALAERFK
3D structure
PDB3x1m Transition of phosphopantetheine adenylyltransferase from catalytic to allosteric state is characterized by ternary complex formation in Pseudomonas aeruginosa
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H17 K41 R90 S128
Catalytic site (residue number reindexed from 1) H17 K41 R90 S128
Enzyme Commision number 2.7.7.3: pantetheine-phosphate adenylyltransferase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 COA B P7 G8 T9 A36 K41 L72 L73 R87 Y97 S127 S128 T129 P7 G8 T9 A36 K41 L72 L73 R87 Y97 S127 S128 T129 MOAD: Ki=6.5uM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004595 pantetheine-phosphate adenylyltransferase activity
GO:0005524 ATP binding
GO:0008771 [citrate (pro-3S)-lyase] ligase activity
GO:0016779 nucleotidyltransferase activity
Biological Process
GO:0009058 biosynthetic process
GO:0015937 coenzyme A biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Cellular Component
External links
PDB RCSB:3x1m, PDBe:3x1m, PDBj:3x1m
PDBsum3x1m
PubMed27041211
UniProtA0A0X1KGP2

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